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Figure 1
Stereoview of the structure of the active site and its vicinity in ferric cytochrome P450cam determined from the unsoaked crystals. Active-site residues (Cys357 and Tyr96), haem (iron represented by a large orange sphere), substrate (+)-camphor, a water molecule (a small red sphere) liganded to haem and Thr101 are shown as stick models (with green C atoms, red O atoms and a blue N atom). (+)-Camphor, the water molecule and Thr101 are represented by electron density from the composite OMIT map (cyan, contoured at 1.5σ). The Thr101 side chain exhibits two rotamer structures. (Note the two red sticks extended in different directions: one toward the hydroxy group of Tyr96 and the other toward the peripheral haem 6-propionate. The electron density of the latter is much higher than that of the former.) It is also noted that the electron density of the keto group of (+)-camphor is much stronger than that of the bound water. Figures were drawn using PyMOL (v.0.99rc6).

ISSN: 2053-230X
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